Identification of Protein Targets of 12/15-Lipoxygenase-Derived Lipid Electrophiles in Mouse Peritoneal Macrophages Using Omega-Alkynyl Fatty Acid

ACS Chem Biol. 2018 Apr 20;13(4):887-893. doi: 10.1021/acschembio.7b01092. Epub 2018 Mar 1.

Abstract

The 12/15-lipoxygenase (12/15-LOX) enzyme introduces peroxyl groups, in a position-specific manner, into polyunsaturated fatty acids to form various kinds of bioactive lipid metabolites, including lipid-derived electrophiles (LDE). The resident peritoneal macrophage is the site of highest 12/15-LOX expression in the mouse. However, the role of the enzyme in the regulation of resident macrophages is not fully understood. Here, we describe a chemoproteomic method to identify the targets of enzymatically generated LDE. By treating mouse peritoneal macrophages with omega-alkynyl arachidonic acid (aAA), we identified a series of proteins adducted by LDE generated through a 12/15-LOX catalyzed reaction. Pathway analysis revealed a dramatic enrichment of proteins involved in energy metabolism and found that glycolytic flux and mitochondrial respiration were significantly affected by the expression of 12/15-LOX. Our findings thus highlight the utility of chemoproteomics using aAA for identifying intracellular targets of enzymatically generated LDE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arachidonate 12-Lipoxygenase / chemistry*
  • Arachidonate 12-Lipoxygenase / metabolism
  • Arachidonate 15-Lipoxygenase / chemistry*
  • Arachidonate 15-Lipoxygenase / metabolism
  • Arachidonic Acid / metabolism
  • Energy Metabolism
  • Fatty Acids, Unsaturated / metabolism*
  • Lipids / chemistry*
  • Macrophages, Peritoneal / chemistry*
  • Mice
  • Proteomics / methods

Substances

  • 12-15-lipoxygenase
  • Fatty Acids, Unsaturated
  • Lipids
  • Arachidonic Acid
  • Arachidonate 12-Lipoxygenase
  • Arachidonate 15-Lipoxygenase